7 research outputs found
A poorer nutritional status impacts quality of life in a sample population of elderly cancer patients
Rationale
Quality of Life (QoL) is impaired in cancer, and the elderly are particularly vulnerable to malnutrition. A diagnosis of cancer in elderly patients further exacerbates risks of negative health outcomes. Here we investigated associations between QoL and nutritional status in a sample population of mostly socially deprived elderly cancer patients.
Method
432 cancer patients were recruited for this cross-sectional study at point of admission to a tertiary referral hospital for cancer treatment. Patient-generated subjective global assessment (PG-SGA) assessed nutritional status. Functional assessment of cancer therapy- general (FACT-G) quantified QoL. Relationship between PG-SGA and QoL was assessed by Spearman correlation. PG-SGA outcomes were compared against FACT-G scores employing Mann–Whitney test. Bivariate Linear Regression Model was employed to investigate influences of sociodemographic, clinical and nutritional status upon QoL.
Results
37.5% of participants were malnourished or at risk. 39% were illiterate and 54.6% had family income lower than minimum wage. Malnourished patients showed lower FACT-G scores (76.8 vs. 84.7; p = 0.000). Poor nutritional diagnosis was inversely correlated with all QoL domains. Bivariate regression analysis showed that lower PG-SGA scores (βo =  − 1.00; p = 0.000) contributed to FACT-G score deterioration, the male gender showed better QoL scores, and other clinical and sociodemographic variables did not show relationship.
Conclusion
Poorer nutritional status was significantly associated with worsened physical, social, emotional and functional well-being QoL domains in elderly cancer patients. Poorer nutritional status is an independent risk factor for worsened QoL. Future policies aimed at particularly vulnerable populations may improve QoL and health outcomes
Prevalence and risk factors for bovine leptospirosis in Mato Grosso do Sul, Brazil
Foi investigada a prevalência de anticorpos antileptospira em fêmeas bovinas com idade igual ou superior a 24 meses, provenientes de 178 rebanhos de 22 municÃpios do estado de Mato Grosso do Sul, bem como identificados fatores de risco associados à infecção. Foram analisadas 2.573 amostras de soro sangüÃneo por meio do teste de soroaglutinação microscópica perante 10 sorovares de leptospira. TÃtulos iguais ou superiores a 100 para um ou mais sorovares foram detectados em 1.801 fêmeas (98,8%) de 161 (96,5%) rebanhos. O sorovar Hardjo (65,6%) foi apontado como o mais provável, seguido do sorovar Wolffi (12,3%). Os resultados demonstram que a leptospirose bovina se encontra presente em todos os municÃpios estudados, com alta prevalência, tanto em animais como em rebanhos. Os fatores de risco identificados neste estudo e associados à infecção por bactérias do gênero lepstopira foram o tipo de exploração pecuária de corte e a raça Zebu. _____________________________________________________________________________________________________________ ABSTRACTThe prevalence of anti-Leptospira spp. antibodies was estimated for female cattle aged 24 months or older. The sample comprised 178 herds from 22 counties in the state of Mato Grosso do Sul, Brazil. The risk factors associated with the presence of infeccion were investigated. A total of 2,573 blood serum samples were tested against 10 leptospira serovars using the microagglutination test (MAT). Titers of 100 or higher for one or more serovars were detected in 1,801 females (98.8%) from 161 herds (96.5%). Serovar Hardjo (65.6%) was the most frequent, followed by serovar Wolffi (12.3%). These results suggest that bovine leptospirosis is widespread in all the counties under study, with a high prevalence both at the animal and the herd level. Beef farms and the Zebu breed were associated to the higher risk of herd infection by leptospiras
Searching for the role of protein phosphatases in eukaryotic microorganisms
Preference for specific protein substrates together with differential sensitivity to activators and inhibitors has allowed classification of serine/threonine protein phosphatases (PPs) into four major types designated types 1, 2A, 2B and 2C (PP1, PP2A, PP2B and PP2C, respectively). Comparison of sequences within their catalytic domains has indicated that PP1, PP2A and PP2B are members of the same gene family named PPP. On the other hand, the type 2C enzyme does not share sequence homology with the PPP members and thus represents another gene family, known as PPM. In this report we briefly summarize some of our studies about the role of serine/threonine phosphatases in growth and differentiation of three different eukaryotic models: Blastocladiella emersonii, Neurospora crassa and Dictyostelium discoideum. Our observations suggest that PP2C is the major phosphatase responsible for dephosphorylation of amidotransferase, an enzyme that controls cell wall synthesis during Blastocladiella emersonii zoospore germination. We also report the existence of a novel acid- and thermo-stable protein purified from Neurospora crassa mycelia, which specifically inhibits the PP1 activity of this fungus and mammals. Finally, we comment on our recent results demonstrating that Dictyostelium discoideum expresses a gene that codes for PP1, although this activity has never been demonstrated biochemically in this organism
Searching for the role of protein phosphatases in eukaryotic microorganisms
Preference for specific protein substrates together with differential sensitivity to activators and inhibitors has allowed classification of serine/threonine protein phosphatases (PPs) into four major types designated types 1, 2A, 2B and 2C (PP1, PP2A, PP2B and PP2C, respectively). Comparison of sequences within their catalytic domains has indicated that PP1, PP2A and PP2B are members of the same gene family named PPP. On the other hand, the type 2C enzyme does not share sequence homology with the PPP members and thus represents another gene family, known as PPM. In this report we briefly summarize some of our studies about the role of serine/threonine phosphatases in growth and differentiation of three different eukaryotic models: Blastocladiella emersonii, Neurospora crassa and Dictyostelium discoideum. Our observations suggest that PP2C is the major phosphatase responsible for dephosphorylation of amidotransferase, an enzyme that controls cell wall synthesis during Blastocladiella emersonii zoospore germination. We also report the existence of a novel acid- and thermo-stable protein purified from Neurospora crassa mycelia, which specifically inhibits the PP1 activity of this fungus and mammals. Finally, we comment on our recent results demonstrating that Dictyostelium discoideum expresses a gene that codes for PP1, although this activity has never been demonstrated biochemically in this organism